Maltose grown cells of Fusobacterium mortiferum ATCC 25557 were able to transport maltose, in contrast to cells from cultures grown on other energy sources. Maltose grown cells were also able to use both maltose and sucrose, as well as a variety of alpha linked glucosyl disaccharides, anaerobically from a buffered cell suspension. Permeabalized cells and sonic extracts of maltose grown F. mortiferum phosphorylate maltose with phosphoenolpyruvate [PEP] exclusively as the phosphate donor. Permeabalized cells from cultures grown on serine, glucose or sucrose were unable to phosphorylate maltose with either adenosine triphosphate [ATP] or PEP as a phosphate donor. PEP stimulated glucose phosphorylation was found in cells grown on all four energy sources and was strongest in maltose grown cells. When a sonic extract of F. mortiferum was resolved into membrane and cytosolic fractions neither component could affect PEP dependent maltose phosphorylation alone but maltose PTS activity was restored by addition of both components. The cystosolic fraction from either glucose or maltose grown cells complimented maltose membranes for maltose PTS activity. A glucose PTS was demonstrated in maltose grown cells. Aerobic conditions allowed PEP dependent maltose phosphorylation but prevented further disaccharide dissimilation suggesting aerobic sensitivity of a putative maltose-6-phosphate hydrolase. Maltose-6-phosphate hydrolase activity could not be demonstrated using cell extracts although evidence with intact anaerobic cells showed conclusively that the activity was present. Maltose-6-phosphate was prepared in milligram amounts using permeabalized maltose grown F. mortiferum, maltose and PEP as described herein. The structure of the compound was proved by chromatographic identification of products following enzymatic and chemical treatments. The proposed structure was confirmed using mass spectral data and nuclear magnetic resonance spectroscopy. Cystathionase [cystine lyase] was detected by activity stain in a gel following separation of sonic extracts of a variety of fusobacteria.